Influenza virus remains one of the most important disease-causing viruses owing to its high adaptability and even higher contagious nature. Thus, it poses a constant threat of pandemic, engulfing a large population within the smallest possible time interval. A similar threat was anticipated with the identification of the novel H7N9 virus in China on 30 March 2013. Detection of transmission of the virus between humans has caused a stir with the identification of family clusters along with sporadic infections all across China. In this review we analyze the potential of the novel H7N9 virus as a probable cause of a pandemic and the possible consequences thereof.

Protists in the phylum Ciliophora possess a complex membrane‐trafficking system, including osmoregulatory Contractile Vacuoles and specialized secretory organelles. Molecular cell biological investigations in Tetrahymena thermophila have identified components of the protein machinery associated with the secretory organelles, mucocysts. The Qa‐SNARE Syn7lp plays a role in mucocyst biogenesis as do subunits of the CORVET tethering complex (specifically Vps8). Indeed, Tetrahymena thermophila possesses expanded gene complements of several CORVET components, including Vps33 which is also a Sec1/Munc18 (SM) protein that binds Qa‐SNAREs. Moreover, the Qa‐SNAREs in Paramecium tetraurelia have been localized to various endomembrane organelles. Here, we use comparative genomics and phylogenetics to determine the evolutionary history of the SM and Qa‐SNARE proteins across the Ciliophora. We identify that the last ciliate common ancestor possessed the four SM proteins and six Qa‐SNAREs common to eukaryotes, including the uncommonly retained Syntaxin 17. We furthermore identify independent expansion of these protein families in several ciliate classes, including concurrent expansions of the SM protein‐Qa SNARE partners Sec1:SynPM in the oligohymenophorean ciliates lineage, consistent with novel Contractile Vacuole specific innovations. Overall, these data are consistent with SM proteins and Qa‐SNAREs being a common set of components for endomembrane modulation in the ciliates.